Header list of 1r5e.pdb file
Complete list - c 21 2 Bytes
HEADER PROTEIN BINDING 10-OCT-03 1R5E
TITLE SOLUTION STRUCTURE OF THE FOLDED CORE OF PSEUDOMONAS SYRINGAE EFFECTOR
TITLE 2 PROTEIN, AVRPTO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AVIRULENCE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRAVRPTO (RESIDUES 29-133);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SYRINGAE;
SOURCE 3 ORGANISM_TAXID: 317;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PFLAG-CTC
KEYWDS THREE-HELIX BUNDLE, OMEGA LOOP, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR J.WULF,P.E.PASCUZZI,G.B.MARTIN,L.K.NICHOLSON
REVDAT 4 21-DEC-22 1R5E 1 SEQADV
REVDAT 3 02-MAR-22 1R5E 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1R5E 1 VERSN
REVDAT 1 19-OCT-04 1R5E 0
JRNL AUTH J.WULF,P.E.PASCUZZI,A.FAHMY,G.B.MARTIN,L.K.NICHOLSON
JRNL TITL THE SOLUTION STRUCTURE OF TYPE III EFFECTOR PROTEIN AVRPTO
JRNL TITL 2 REVEALS CONFORMATIONAL AND DYNAMIC FEATURES IMPORTANT FOR
JRNL TITL 3 PLANT PATHOGENESIS.
JRNL REF STRUCTURE V. 12 1257 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15242602
JRNL DOI 10.1016/J.STR.2004.04.017
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER, STEIN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL OF 1898
REMARK 3 RESTRAINTS, 1584 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 206
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,108 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS
REMARK 4
REMARK 4 1R5E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020458.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 15MM PHOSPHATE, 245MM SODIUM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM TRAVRPTO U-15N;10MM NA2HPO4
REMARK 210 5MM KH2PO4 225MM NACL PH6; 1MM
REMARK 210 TRAVRPTO U-15N,13C;10MM NA2HPO4
REMARK 210 5MM KH2PO4 225MM NACL PH6; 1MM
REMARK 210 TRAVRPTO U-15N,13C;10MM NA2HPO4
REMARK 210 5MM KH2PO4 225MM NACL PH6
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, PIPP
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 MET A 28
REMARK 465 VAL A 134
REMARK 465 ASP A 135
REMARK 465 TYR A 136
REMARK 465 LYS A 137
REMARK 465 ASP A 138
REMARK 465 ASP A 139
REMARK 465 ASP A 140
REMARK 465 ASP A 141
REMARK 465 LYS A 142
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 PRO A 50 -82.51 -56.42
REMARK 500 1 ARG A 51 -68.57 -148.63
REMARK 500 1 GLN A 60 -67.24 -123.95
REMARK 500 1 ALA A 61 151.24 -39.97
REMARK 500 1 MET A 85 -49.58 -130.18
REMARK 500 1 HIS A 87 71.22 -67.71
REMARK 500 1 THR A 91 -167.74 -103.46
REMARK 500 1 ALA A 93 34.47 -94.28
REMARK 500 1 SER A 94 -114.44 -99.47
REMARK 500 1 ASN A 97 166.71 -47.15
REMARK 500 1 PRO A 98 55.22 -68.73
REMARK 500 2 PRO A 50 -85.44 -65.47
REMARK 500 2 ARG A 51 -78.36 -148.34
REMARK 500 2 GLN A 60 -63.68 -126.36
REMARK 500 2 MET A 85 -45.76 -130.22
REMARK 500 2 ALA A 93 34.17 -94.21
REMARK 500 2 SER A 94 -114.62 -99.79
REMARK 500 3 ALA A 47 -167.70 -77.75
REMARK 500 3 PRO A 50 -79.31 -60.69
REMARK 500 3 ARG A 51 -69.32 -148.18
REMARK 500 3 GLN A 60 -67.61 -123.89
REMARK 500 3 ALA A 61 150.82 -39.26
REMARK 500 3 TYR A 69 -71.55 -54.47
REMARK 500 3 ASP A 84 38.66 -90.90
REMARK 500 3 MET A 85 -46.59 -130.44
REMARK 500 3 MET A 90 -72.99 -69.50
REMARK 500 3 SER A 94 -179.43 -176.54
REMARK 500 3 PRO A 98 40.87 -87.16
REMARK 500 4 PRO A 50 -77.45 -55.93
REMARK 500 4 ARG A 51 -70.43 -148.70
REMARK 500 4 GLN A 60 -63.68 -127.27
REMARK 500 4 ALA A 61 150.74 -40.47
REMARK 500 4 ASP A 84 40.94 -91.43
REMARK 500 4 MET A 85 -40.47 -130.50
REMARK 500 4 HIS A 87 -160.23 -62.28
REMARK 500 4 ARG A 88 -64.32 -131.39
REMARK 500 4 ALA A 93 34.12 -92.72
REMARK 500 4 SER A 94 -114.74 -103.83
REMARK 500 4 PRO A 98 56.83 -69.10
REMARK 500 5 PRO A 50 -83.45 -60.57
REMARK 500 5 ARG A 51 -71.14 -148.17
REMARK 500 5 GLN A 60 -62.62 -129.43
REMARK 500 5 ALA A 61 150.48 -42.62
REMARK 500 5 ASP A 84 35.48 -96.22
REMARK 500 5 MET A 85 -51.70 -130.87
REMARK 500 5 HIS A 87 71.36 -65.06
REMARK 500 5 THR A 91 137.64 -176.85
REMARK 500 5 ALA A 93 35.80 22.17
REMARK 500 5 PRO A 98 56.97 -69.39
REMARK 500 5 ASP A 132 79.88 -150.05
REMARK 500
REMARK 500 THIS ENTRY HAS 309 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1R5E A 29 133 UNP Q08242 Q08242_PSESX 29 133
SEQADV 1R5E MET A 28 UNP Q08242 CLONING ARTIFACT
SEQADV 1R5E VAL A 134 UNP Q08242 CLONING ARTIFACT
SEQADV 1R5E ASP A 135 UNP Q08242 EXPRESSION TAG
SEQADV 1R5E TYR A 136 UNP Q08242 EXPRESSION TAG
SEQADV 1R5E LYS A 137 UNP Q08242 EXPRESSION TAG
SEQADV 1R5E ASP A 138 UNP Q08242 EXPRESSION TAG
SEQADV 1R5E ASP A 139 UNP Q08242 EXPRESSION TAG
SEQADV 1R5E ASP A 140 UNP Q08242 EXPRESSION TAG
SEQADV 1R5E ASP A 141 UNP Q08242 EXPRESSION TAG
SEQADV 1R5E LYS A 142 UNP Q08242 EXPRESSION TAG
SEQRES 1 A 115 MET ASP ASN VAL THR SER SER GLN LEU LEU SER VAL ARG
SEQRES 2 A 115 HIS GLN LEU ALA GLU SER ALA GLY LEU PRO ARG ASP GLN
SEQRES 3 A 115 HIS GLU PHE VAL SER SER GLN ALA PRO GLN SER LEU ARG
SEQRES 4 A 115 ASN ARG TYR ASN ASN LEU TYR SER HIS THR GLN ARG THR
SEQRES 5 A 115 LEU ASP MET ALA ASP MET GLN HIS ARG TYR MET THR GLY
SEQRES 6 A 115 ALA SER GLY ILE ASN PRO GLY MET LEU PRO HIS GLU ASN
SEQRES 7 A 115 VAL ASP ASP MET ARG SER ALA ILE THR ASP TRP SER ASP
SEQRES 8 A 115 MET ARG GLU ALA LEU GLN HIS ALA MET GLY ILE HIS ALA
SEQRES 9 A 115 ASP ILE VAL ASP TYR LYS ASP ASP ASP ASP LYS
HELIX 1 1 THR A 32 ALA A 47 1 16
HELIX 2 2 ARG A 51 SER A 58 1 8
HELIX 3 3 PRO A 62 ASP A 84 1 23
HELIX 4 4 LEU A 101 ILE A 129 1 29
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - c 21 2 Bytes